2O3O

Crystal Structure of the sensor histidine kinase regulator YycI from Bacillus subtitlis

Summary for 2O3O

• Entry DOI: 10.2210/pdb2o3o/pdb
• Descriptor: YycI protein, CHLORIDE ION (2 entities in total)
• Functional Keywords: two-component system, signaling protein
• Biological source: Bacillus subtilis
• Cellular location: Cell membrane; Single-pass membrane protein (Potential): Q45612
• Total number of polymer chains: 12
• Total formula weight: 355848.53

Authors

Santelli, E.,Liddington, R.C. (deposition date: 2006-12-01, release date: 2007-04-10, Last modification date: 2024-10-16)

Primary citation

Santelli, E.,Liddington, R.C.,Mohan, M.A.,Hoch, J.A.,Szurmant, H.
The Crystal Structure of Bacillus subtilis YycI Reveals a Common Fold for Two Members of an Unusual Class of Sensor Histidine Kinase Regulatory Proteins.
J.Bacteriol., 189:3290-3295, 2007

PubMed Abstract: YycI and YycH are two membrane-anchored periplasmic proteins that regulate the essential Bacillus subtilis YycG histidine kinase through direct interaction. Here we present the crystal structure of YycI at a 2.9-A resolution. YycI forms a dimer, and remarkably the structure resembles that of the two C-terminal domains of YycH despite nearly undetectable sequence homology (10%) between the two proteins.

PubMed: 17307848
DOI: 10.1128/JB.01937-06

Experimental method

X-RAY DIFFRACTION (2.89 Å)